Interactions between DNA and hen's egg white lysozyme: Effects of composition and structural changes of DNA, ionic strength and temperature

Markedly increased quantities of lysozyme have been found in the serum and urine (ranging to 2.6 g per day) of ten consecutive cases of monocytic and monomyelocytic leukemia. The enzyme has been isolated from the urine of several cases and physicochemically and immunochemically characterized. It is apparently identical to the lysozyme of normal tears, saliva, leukocytes, and serum, but structurally different from the lysozyme of hen's egg white. The activity of the human enzyme assayed with M. lysodeikticus organisms is 3 to 12 times greater than egg white lysozyme at equivalent concentrations. An agar plate method has been developed for quantitating lysozyme activity in small samples (approximately 25 µl) of serum, urine, or other biological fluids. The range and reproducibility of this method were found to be superior to previously available lysozyme assay procedures. Present evidence indicates that lysozyme is the principal, if not the sole, product of the proliferating monocytes in monocytic and monomyelocytic leukemia, and quantitation of serum and urine lysozyme should be a useful diagnostic procedure for these leukemias.

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The precise and entire antigenic structure of native lysozyme

Biochemical Journal ◽

10.1042/bj1710429 ◽

1978 ◽

Vol 171 (2) ◽

pp. 429-434 ◽

Cited By ~ 85

Author(s):

M Z Atassi ◽

C L Lee

Keyword(s):

Egg White ◽

Antigenic Structure ◽

Egg White Lysozyme ◽

Antigenic Sites ◽

Exact Boundary ◽

Hen’S Egg ◽

Antigenic Reactivity

The exact boundary, residue, conformational and directional definitions of the three antigenic sites of native hen's egg-white lysozyme are described. The results clearly reveal that the three antigenic sites account quantitatively for the total antigenic reactivity of the protein. Thus the entire antigenic structure of lysozyme has now been precisely determined and is briefly discussed here, together with the power of the surface-stimulation synthetic concept.

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Influence of the ionic strength on the amyloid fibrillogenesis of hen egg white lysozyme

International Journal of Biological Macromolecules ◽

10.1016/j.ijbiomac.2018.09.165 ◽

2019 ◽

Vol 121 ◽

pp. 63-70 ◽

Cited By ~ 5

Author(s):

Jarosław Wawer ◽

Michał Szociński ◽

Marcin Olszewski ◽

Rafał Piątek ◽

Mateusz Naczk ◽

...

Keyword(s):

Ionic Strength ◽

Egg White ◽

Hen Egg White Lysozyme ◽

Egg White Lysozyme ◽

Hen Egg White ◽

Hen Egg

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FRACTIONATION AND DISSOCIATION OF THE AVIAN LIPOVITELLINS AND THEIR INTERACTION WITH PHOSVITIN

Canadian Journal of Biochemistry ◽

10.1139/o64-047 ◽

1964 ◽

Vol 42 (3) ◽

pp. 395-406 ◽

Cited By ~ 15

Author(s):

M. W. Radomski ◽

W. H. Cook

Keyword(s):

Ionic Strength ◽

Phosphate Buffer ◽

Structural Changes ◽

Phosphorus Content ◽

Egg Yolk ◽

Gradient Elution ◽

Progressive Change ◽

Hen’S Egg ◽

Dowex 1 ◽

Elution Chromatography

Phosvitin and lipovitellin, the granule proteins of hen's egg yolk, were clearly separated by gradient elution on Dowex-1 columns. No phosvitin could be detected in the lipovitellin fraction but the first eluates of the phosvitin fraction contained lipovitellin of high protein phosphorus content. These initial eluates contained only two components sedimenting at rates slightly higher than dimer and monomer lipovitellin. As the lipovitellin monomer does not ordinarily occur in neutral solvents, the slower sedimenting material is either a new component or the monomer stabilized through interaction with phosvitin.Gradient elution chromatography of the total lipovitellins on hydroxyapatite showed that β-lipovitellin was completely eluted by 0.6 M phosphate buffer at pH 6.8 and appeared to be homogeneous. However, α-lipovitellin was heterogeneous: it was eluted over a concentration range of 0.7 to 1.4 M and the protein phosphorus content and dissociative behavior of successive fractions showed a progressive change with increasing ionic strength. Superimposed on this general heterogeneity of α-lipovitellin, there was consistent evidence of two poorly defined components, and three when the α-fraction was rechromatographed. Following dissociation and reassociation, there was no evidence of hybridization between monomers of α- and β-lipovitellin. Changes in the chromatographic patterns of α-lipovitellin following dissociation may indicate hybridization of different α-monomers, but these could also arise from structural changes in the monomers.

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